Phosphorylation of Both Serine Residues in Cardiac Troponin I Is Required to Decrease the Ca2+ Affinity of Cardiac Troponin C
Open Access
- 1 December 1995
- journal article
- Published by Elsevier
- Vol. 270 (51) , 30773-30780
- https://doi.org/10.1074/jbc.270.51.30773
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation.Circulation Research, 1994
- A common motif of two adjacent phosphoserines in bovine, rabbit and human cardiac troponin IFEBS Letters, 1990
- Sites phosphorylated in bovine cardiac troponin T and IEuropean Journal of Biochemistry, 1990
- Cardiac troponin I, isolated from‐bovine heart, contains two adjacent phosphoserinesEuropean Journal of Biochemistry, 1988
- Amino acid sequence of bovine cardiac troponin IBiochemistry, 1988
- Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit heartsBiochemical Journal, 1988
- Structural Aspects of Troponin-Tropomyosin Regulation of Skeletal Muscle ContractionAnnual Review of Biophysics, 1987
- Phosphorylation of C-protein in intact amphibian cardiac muscle. Correlation between 32P incorporation and twitch relaxation.The Journal of general physiology, 1984
- Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heartNature, 1976
- Relaxing and inotropic effects of cyclic AMP on skinned cardiac cellsNature, 1975